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The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Lysosomes01:31

Lysosomes

Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...

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Related Experiment Video

Updated: May 29, 2026

Measuring Calpain Activity in Fixed and Living Cells by Flow Cytometry
11:37

Measuring Calpain Activity in Fixed and Living Cells by Flow Cytometry

Published on: July 8, 2010

Calpains: an elaborate proteolytic system.

Yasuko Ono1, Hiroyuki Sorimachi

  • 1Calpain Project, Department of Advanced Science for Biomolecules, Tokyo Metropolitan Institute of medical Science, Tokyo, Japan. ono-ys@igakuken.or.jp

Biochimica Et Biophysica Acta
|August 26, 2011
PubMed
Summary
This summary is machine-generated.

Calpains are evolutionarily conserved Ca(2+)-dependent proteases found in most eukaryotes. Their activation mechanism involves two core domains fusing upon calcium binding, enabling shared function despite diverse structures.

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Last Updated: May 29, 2026

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11:37

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Evaluation of Protein&#8211;Protein Interactions using an On-Membrane Digestion Technique
07:07

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Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments
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Published on: July 5, 2014

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Calpains are intracellular calcium-dependent cysteine proteases.
  • They are widely distributed across eukaryotes and some bacteria, indicating evolutionary conservation.
  • Human genome encodes fifteen calpain-like protease domains, with some exhibiting similarity to distant homologs.

Purpose of the Study:

  • To review recent advancements in calpain research.
  • To elucidate the conserved mechanism of calpain activation.
  • To highlight shared mechanistic characteristics among diverse calpain homologs.

Main Methods:

  • Analysis of evolutionary sequence data.
  • Three-dimensional structural analyses of calpain domains.
  • Review of recent experimental studies on calpain function.

Main Results:

  • Calpains are ancient proteases present throughout evolution.
  • Activation mechanism involves two core domains fusing upon Ca(2+) binding.
  • Calpains share a common activation mechanism despite divergent domain structures and independent regulation.

Conclusions:

  • Calpains possess a conserved activation mechanism essential for their function.
  • Structural and sequence data reveal evolutionary persistence and functional unity.
  • Understanding calpain activation provides insights into proteolysis.